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Q9Y657 (SPIN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Spindlin-1
Alternative name(s):
Ovarian cancer-related protein
Spindlin1
Gene names
Name:SPIN1
Synonyms:OCR, SPIN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length262 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Chromatin reader that specifically recognizes and binds histone H3 both trimethylated at 'Lys-4' and asymmetrically dimethylated at 'Arg-8' (H3K4me3 and H3R8me2a) and acts as an activator of Wnt signaling pathway dowstream of PRMT2. In case of cancer, promotes cell cancer proliferation via activation of the Wnt signaling pathway (Ref.18). Overexpression induces metaphase arrest and chromosomal instability. Localizes to active rDNA loci and promotes the expression of rRNA genes (Ref.14). May play a role in cell-cycle regulation during the transition from gamete to embryo. Involved in oocyte meiotic resumption, a process that takes place before ovulation to resume meiosis of oocytes blocked in prophase I: may act by regulating maternal transcripts to control meiotic resumption. Ref.14 Ref.15 Ref.18

Subunit structure

Homodimer; may form higher-order oligomers (Ref.16). Interacts with TCF7L2/TCF4; the interaction is direct. Interacts with HABP4 and SERBP1. Ref.15 Ref.16 Ref.18

Subcellular location

Nucleus. Nucleusnucleolus Ref.3 Ref.14.

Tissue specificity

Highly expressed in ovarian cancer tissues. Ref.15

Domain

The 3 tudor-like domains (also named Spin/Ssty repeats) specifically recognize and bind methylated histones (Ref.17, Ref.18). H3K4me3 and H3R8me2a are recognized by tudor-like domains 2 and 1, respectively (Ref.18). Ref.16

Post-translational modification

Phosphorylated during oocyte meiotic maturation By similarity. Ref.15

Sequence similarities

Belongs to the SPIN/STSY family.

Sequence caution

The sequence AAD43035.1 differs from that shown. Reason: Frameshift at position 21.

The sequence AAG38112.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAG48367.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAB66653.1 differs from that shown. Reason: Erroneous termination at position 171. Translated as Glu.

The sequence CAG38515.1 differs from that shown. Reason: Erroneous termination at position 171. Translated as Glu.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 262262Spindlin-1
PRO_0000181367

Regions

Region53 – 11664Tudor-like domain 1
Region93 – 986Histone H3K4me3 and H3R8me2a binding
Region132 – 19362Tudor-like domain 2
Region1421Histone H3K4me3 and H3R8me2a binding
Region213 – 26250Tudor-like domain 3
Region250 – 2523Histone H3K4me3 and H3R8me2a binding

Sites

Binding site1731Histone H3K4me3 and H3R8me2a
Binding site1801Histone H3K4me3 and H3R8me2a
Binding site1841Histone H3K4me3 and H3R8me2a

Amino acid modifications

Modified residue441N6-acetyllysine By similarity
Modified residue1091Phosphoserine; by AURKA Ref.15
Modified residue1241Phosphoserine; by AURKA Ref.11 Ref.12 Ref.15
Modified residue1991Phosphoserine Ref.11

Natural variations

Natural variant2211A → P.
Corresponds to variant rs34794905 [ dbSNP | Ensembl ].
VAR_053690

Experimental info

Mutagenesis721W → A or R: Impaired binding to histone H3K4me3 and H3R8me2a and impaired ability to activate the Wnt signaling pathway. Ref.18
Mutagenesis981Y → R: Impaired binding to histone H3K4me3 and H3R8me2a and impaired ability to activate the Wnt signaling pathway. Ref.18
Mutagenesis1091S → A: Impaired phosphorylation. Ref.15
Mutagenesis1241S → A: Impaired phosphorylation. Ref.15
Mutagenesis1411F → A: Impaired binding to histone H3K4me3 and H3R8me2a and impaired ability to activate the Wnt signaling pathway. Impaired ability to activate expression of pre-rRNA. Ref.14 Ref.18
Mutagenesis1421E → A: Impaired binding to histone H3K4me3 and H3R8me2a. Ref.18
Mutagenesis1701Y → A: Impaired binding to histone H3K4me3 and H3R8me2a and impaired ability to activate the Wnt signaling pathway. Impaired ability to activate expression of pre-rRNA. Ref.14 Ref.18
Mutagenesis1771Y → A: Impaired binding to histone H3K4me3 and H3R8me2a. Ref.18
Mutagenesis1841D → A or R: Impaired binding to histone H3K4me3 and H3R8me2a. Ref.17 Ref.18
Mutagenesis1891D → A or R: Impaired binding to histone H3K4me3. Ref.17
Mutagenesis2511F → R: Impaired binding to histone H3K4me3 and H3R8me2a and impaired ability to activate the Wnt signaling pathway. Ref.18
Sequence conflict491P → S in BAG52466. Ref.6

Secondary structure

............................................. 262
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Y657 [UniParc].

Last modified April 18, 2006. Version 3.
Checksum: 49F86CBCC7A0AA01

FASTA26229,601
        10         20         30         40         50         60 
MKTPFGKTPG QRSRADAGHA GVSANMMKKR TSHKKHRSSV GPSKPVSQPR RNIVGCRIQH 

        70         80         90        100        110        120 
GWKEGNGPVT QWKGTVLDQV PVNPSLYLIK YDGFDCVYGL ELNKDERVSA LEVLPDRVAT 

       130        140        150        160        170        180 
SRISDAHLAD TMIGKAVEHM FETEDGSKDE WRGMVLARAP VMNTWFYITY EKDPVLYMYQ 

       190        200        210        220        230        240 
LLDDYKEGDL RIMPDSNDSP PAEREPGEVV DSLVGKQVEY AKEDGSKRTG MVIHQVEAKP 

       250        260 
SVYFIKFDDD FHIYVYDLVK TS 

« Hide

References

« Hide 'large scale' references
[1]Peng Y., Song H., Dai M., Huang Q., Mao Y., Zhang Q., Mao M., Fu G., Luo M., Chen J., Hu R.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pituitary.
[2]"Cloning, characterization and mapping of human SPIN to human chromosome 9q22.1-22.3."
Zhang H.L., Yu L., Wang X., Chen Z., Tu Q., Chen J.Q., Ding J.B., Gao J., Zhao S.Y.
Chin. Sci. Bull. 45:909-914(2000)
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Spindlin1, a novel nuclear protein with a role in the transformation of NIH3T3 cells."
Gao Y., Yue W., Zhang P., Li L., Xie X., Yuan H., Chen L., Liu D., Yan F., Pei X.
Biochem. Biophys. Res. Commun. 335:343-350(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
Tissue: Ovarian carcinoma.
[4]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Fetal kidney.
[5]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Amygdala, Hippocampus and Trachea.
[7]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Uterus.
[10]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-225.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Nucleolar protein Spindlin1 recognizes H3K4 methylation and stimulates the expression of rRNA genes."
Wang W., Chen Z., Mao Z., Zhang H., Ding X., Chen S., Zhang X., Xu R., Zhu B.
EMBO Rep. 12:1160-1166(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-141 AND TYR-170.
[15]"SPINDLIN1 promotes cancer cell proliferation through activation of WNT/TCF-4 signaling."
Wang J.X., Zeng Q., Chen L., Du J.C., Yan X.L., Yuan H.F., Zhai C., Zhou J.N., Jia Y.L., Yue W., Pei X.T.
Mol. Cancer Res. 10:326-335(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TCF7L2, PHOSPHORYLATION AT SER-109 AND SER-124, MUTAGENESIS OF SER-109 AND SER-124, TISSUE SPECIFICITY.
[16]"Structure of human spindlin1. Tandem tudor-like domains for cell cycle regulation."
Zhao Q., Qin L., Jiang F., Wu B., Yue W., Xu F., Rong Z., Yuan H., Xie X., Gao Y., Bai C., Bartlam M., Pei X., Rao Z.
J. Biol. Chem. 282:647-656(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 26-262 IN COMPLEX WITH PHOSPHATE IONS, DNA-BINDING, SUBUNIT, DOMAINS TUDOR-LIKE.
[17]"Distinct mode of methylated lysine-4 of histone H3 recognition by tandem tudor-like domains of Spindlin1."
Yang N., Wang W., Wang Y., Wang M., Zhao Q., Rao Z., Zhu B., Xu R.M.
Proc. Natl. Acad. Sci. U.S.A. 109:17954-17959(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 27-262 IN COMPLEX WITH METHYLATED HISTONE H3, MUTAGENESIS OF ASP-184 AND ASP-189.
[18]"Molecular basis underlying histone H3 lysine-arginine methylation pattern readout by Spin/Ssty repeats of Spindlin1."
Su X., Zhu G., Ding X., Lee S.Y., Dou Y., Zhu B., Wu W., Li H.
Genes Dev. 28:622-636(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 50-262 IN COMPLEX WITH METHYLATED HISTONE H3, FUNCTION, INTERACTION WITH TCF7L2, MUTAGENESIS OF TRP-72; TYR-98; PHE-141; GLU-142; TYR-170; TYR-177; ASP-184 AND PHE-251.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF106682 mRNA. Translation: AAD43035.1. Frameshift.
AF087864 mRNA. Translation: AAG48367.1. Different initiation.
AF317228 mRNA. Translation: AAG38112.1. Different initiation.
AL136719 mRNA. Translation: CAB66653.1. Sequence problems.
BT007314 mRNA. Translation: AAP35978.1.
AK092017 mRNA. Translation: BAG52466.1.
AK289691 mRNA. Translation: BAF82380.1.
AK290009 mRNA. Translation: BAF82698.1.
AK315854 mRNA. Translation: BAF98745.1.
AL353748 Genomic DNA. Translation: CAH72406.1.
CH471089 Genomic DNA. Translation: EAW62753.1.
BC013571 mRNA. No translation available.
BC114515 mRNA. Translation: AAI14516.1.
BC114565 mRNA. Translation: AAI14566.1.
CR533484 mRNA. Translation: CAG38515.1. Sequence problems.
CCDSCCDS43843.1.
RefSeqNP_006708.2. NM_006717.2.
UniGeneHs.146804.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2NS2X-ray2.20A/B26-262[»]
4H75X-ray2.10A27-262[»]
4MZFX-ray2.10B50-262[»]
4MZGX-ray1.70B/D50-262[»]
4MZHX-ray2.20A50-262[»]
ProteinModelPortalQ9Y657.
SMRQ9Y657. Positions 50-260.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116130. 15 interactions.
DIPDIP-40062N.
IntActQ9Y657. 6 interactions.
MINTMINT-1428826.
STRING9606.ENSP00000365019.

PTM databases

PhosphoSiteQ9Y657.

Polymorphism databases

DMDM93141317.

Proteomic databases

MaxQBQ9Y657.
PaxDbQ9Y657.
PRIDEQ9Y657.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375859; ENSP00000365019; ENSG00000106723.
ENST00000541629; ENSP00000441864; ENSG00000106723.
GeneID10927.
KEGGhsa:10927.
UCSCuc004apy.3. human.

Organism-specific databases

CTD10927.
GeneCardsGC09P091003.
HGNCHGNC:11243. SPIN1.
HPAHPA000162.
MIM609936. gene.
neXtProtNX_Q9Y657.
PharmGKBPA162404504.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG40069.
HOGENOMHOG000293367.
HOVERGENHBG000686.
InParanoidQ9Y657.
OMAHKDERVQ.
OrthoDBEOG7CK37K.
PhylomeDBQ9Y657.
TreeFamTF332665.

Gene expression databases

BgeeQ9Y657.
CleanExHS_SPIN1.
GenevestigatorQ9Y657.

Family and domain databases

InterProIPR003671. Spin_Ssty.
[Graphical view]
PANTHERPTHR10405. PTHR10405. 1 hit.
PfamPF02513. Spin-Ssty. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSPIN1. human.
EvolutionaryTraceQ9Y657.
GeneWikiSPIN1.
GenomeRNAi10927.
NextBio41511.
PROQ9Y657.
SOURCESearch...

Entry information

Entry nameSPIN1_HUMAN
AccessionPrimary (citable) accession number: Q9Y657
Secondary accession number(s): A8K0X6 expand/collapse secondary AC list , B3KRQ4, Q7KZJ8, Q9GZT2, Q9H0N7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: April 18, 2006
Last modified: July 9, 2014
This is version 105 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM